ISSN: 1001-0602
EISSN: 1748-7838
2012 impact factor 10.526*
(Thomson Reuters, 2013)
Free Sample Issue
 

VOLUME 29 ISSUE 9(9,2019): 694-695

 

Histone lysine de-β-hydroxybutyrylation by SIRT3

 

Susan M. Abmayr 1,2 and Jerry L. Workman 1

 

1The Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA and 2Department of Anatomy and Cell Biology, University of Kansas School of Medicine, Kansas City, KS 66160, USA

Correspondence:Jerry L. Workman (JLW@stowers.org)        

 

Recent studies have demonstrated the addition and removal of a smorgasbord of site-specific acylation modifications on lysine residues of histone tails. The study by Zhang et al. now shows how the SIRT3 histone deacylase exhibits class specificity, acting on only a subset of β-hydroxybutyrylated lysines.

 

https://doi.org/10.1038/s41422-019-0211-2

 
 
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